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A selective inhibitor of cyclic AMP‐dependent protein kinase, N ‐[2‐bromocinnamyl(amino)ethyl]‐5‐isoquinolinesulfonamide (H‐89), inhibits phosphatidylcholine biosynthesis in HeLa cells
Author(s) -
Geilen Christoph C.,
Wieprecht Marcus,
Wieder Thomas,
Reutter Werner
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80811-t
Subject(s) - phosphatidylcholine , forskolin , protein kinase a , protein kinase inhibitor , choline kinase , choline , hela , biosynthesis , biochemistry , chemistry , enzyme inhibitor , kinase , biology , phospholipid , enzyme , membrane , in vitro
In this study, we report that the potent and selective inhibitor of cyclic AMP‐dependent protein kinase, N ‐[2‐bromocinnamyl(amino)ethyl]‐5‐isoquinolinesulfonamide (H‐89) interferes with the incorporation of choline into phosphatidylcholine in HeLa cells. Treatment of cells with 10 μM H‐89 for 1 h decreases the phosphatidylcholine biosynthesis by 50%. This inhibition is prevented by simultaneous addition of 10 μM forskolin, while the choline uptake itself is not affected by H‐89.